Iron-Sulfur Protein Assembly in Human Cells.
Rev Physiol Biochem Pharmacol
; 174: 25-65, 2018.
Article
in En
| MEDLINE
| ID: mdl-28828516
ABSTRACT
Iron-sulfur (Fe-S) clusters serve as a fundamental inorganic constituent of living cells ranging from bacteria to human. The importance of Fe-S clusters is underscored by their requirement as a co-factor for the functioning of different enzymes and proteins. The biogenesis of Fe-S cluster is a highly coordinated process which requires specialized cellular machinery. Presently, understanding of Fe-S cluster biogenesis in human draws meticulous attention since defects in the biogenesis process result in development of multiple diseases with unresolved solutions. Mitochondrion is the major cellular compartment of Fe-S cluster biogenesis, although cytosolic biogenesis machinery has been reported in eukaryotes, including in human. The core biogenesis pathway comprises two steps. The process initiates with the assembly of Fe-S cluster on a platform scaffold protein in the presence of iron and sulfur donor proteins. Subsequent process is the transfer and maturation of the cluster to a bonafide target protein. Human Fe-S cluster biogenesis machinery comprises the mitochondrial iron-sulfur cluster (ISC) assembly and export system along with the cytosolic Fe-S cluster assembly (CIA) machinery. Impairment in the Fe-S cluster machinery components results in cellular dysfunction leading to various mitochondrial pathophysiological consequences. The current review highlights recent developments and understanding in the domain of Fe-S cluster assembly biology in higher eukaryotes, particularly in human cells.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Mitochondrial Proteins
/
Iron-Sulfur Proteins
/
Mitochondria
Limits:
Humans
Language:
En
Journal:
Rev Physiol Biochem Pharmacol
Year:
2018
Document type:
Article
Affiliation country:
India